Determination of catalase activity in samples treated with [ZnCl2(isopropylamine)(2)]: a novel zinc complex that slows down the decay in activity of catalase extracts

Garcia Canadas, Jorge, Perez, J. M., Quiroga, A. G., Fuertes, M. A., Alonso, C. and Navarro-Ranninger, C. 2002. Determination of catalase activity in samples treated with [ZnCl2(isopropylamine)(2)]: a novel zinc complex that slows down the decay in activity of catalase extracts. Journal of the Chemical Society, Dalton Transactions (11) , pp. 2283-2288. 10.1039/B201151B

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Abstract

Reaction of ZnCl2 with an excess of isopropylamine ligand in water gives [ZnCl2(isopropylamine)2]. This novel zinc complex has been characterized by elemental analysis and 1H-NMR. Interestingly, we have found that [ZnCl2(isopropylamine)2] markedly retards the decay in activity of catalase extracts. In fact, catalase extracts (0.075 mg of protein ml−1) may retain more than 80% of their initial enzymatic activity within the first 10 hours of incubation with 0.10 μM [ZnCl2(isopropylamine)2] while the activity of control extracts decreases to less than 50% of the initial value. Moreover, after 24 hours of treatment with [ZnCl2(isopropylamine)2] under the above-mentioned conditions, 70% of the initial enzymatic activity is still retained by catalase extracts while the activity of control untreated extracts drops to 17% of the initial value. On the other hand, our results show that after incubation of catalase extracts with [ZnCl2(isopropylamine)2] the supernatants obtained by centrifugation of the extracts contain a higher amount of active catalase than the supernatants of control untreated catalase extracts. Moreover, [ZnCl2(isopropylamine)2] induces precipitation of a large amount of contaminant proteins present in the catalase extracts. Altogether, these data indicate that treatment of catalase extracts with [ZnCl2(isopropylamine)2] both increases the pureness of catalase solutions and slows down the decay in catalase activity. We believe that [ZnCl2(isopropylamine)2] may be useful as a stabilizing agent for enzyme activity assays with crude catalase extracts.

Item Type:	Article
Date Type:	Publication
Status:	Published
Schools:	Engineering
Subjects:	Q Science > QD Chemistry T Technology > TA Engineering (General). Civil engineering (General)
Publisher:	Royal Society of Chemistry
ISSN:	1472-7773
Last Modified:	19 Mar 2016 23:21
URI:	https://orca.cardiff.ac.uk/id/eprint/48396

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